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Literature summary for 3.4.23.16 extracted from

  • Eizert, H.; Bander, P.; Bagossi, P.; Sperka, T.; Miklossy, G.; Boross, P.; Weber, I.T.; Toezser, J.
    Amino acid preferences of retroviral proteases for amino-terminal positions in a type 1 cleavage site (2008), J. Virol., 82, 10111-10117.
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 1
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information comparison of protease specificities for P1, P3, P4 cleaving positions of proteases of HIV-1, HIV-2, equine infectious anemia virus, avian myeloblastosis virus, Mason-Pfizer monkey virus, mouse mammary tumor virus, Moloney murine leukemia virus, human T-lymphotropic virus type 1, bovine leukemia virus, walleye dermal sarcoma virus, and human foamy virus. The retroviral proteases have similar preferences for Phe and Tyr for the P1 position in this sequence context. The sizes of the P3 and P4 residues appear to be a major contributor for specificity Human immunodeficiency virus 1 ?
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